Hijack of ubiquitination by SARS-CoV-2 (WP4860)
SARS-CoV-2 includes a novel Orf10 that interacts with muliple members of the Cullin 2 ubiquitin ligase complex as determined by AP-MS (Gordon 2020). The strongest interaction is with ZYG11B, a substrate adaptor for CUL2. By binding this complex, Orf10 might be able to hijack its activity. The hijacking of ubiquitination machinery is a common strategy of viruses to direct the degradation of viral restriction factors, for example. Also depicted here is the required neddylation (N8) of CUL2 by the NAE enzyme complex. The ability of this enzyme to transfer N8 to CUL2 is inhibited by the small molecule Pevonedistat.
AuthorsAlex Pico , Egon Willighagen , Finterly Hu , Eric Weitz , Martina Summer-Kutmon , and Isabel Wassink
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OrganismsHomo sapiens COVID-19
Disease OntologyCOVID-19 severe acute respiratory syndrome viral infectious disease
Pathway Ontologyregulatory pathway altered ubiquitin/proteasome degradation pathway disease pathway
Cell Type Ontologyperipheral blood mononuclear cell
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